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dc.contributor.author
Pérez de Berti, Federico Javier
dc.contributor.author
Capaldi, Stefano
dc.contributor.author
Ferreyra, Raul Gabriel
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Burgardt, Noelia Ines
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Acierno, Juan Pablo
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Klinke, Sebastian
dc.contributor.author
Monaco, Hugo L.
dc.contributor.author
Ermacora, Mario Roberto
dc.date.available
2017-07-06T13:45:38Z
dc.date.issued
2013-12
dc.identifier.citation
Pérez de Berti, Federico Javier; Capaldi, Stefano; Ferreyra, Raul Gabriel; Burgardt, Noelia Ines; Acierno, Juan Pablo; et al.; The crystal structure of sterol carrier protein 2 from Yarrowia lipolytica and the evolutionary conservation of a large, non-specific lipid-binding cavity; Springer; Journal of Structural and Functional Genomics; 14; 4; 12-2013; 145-153
dc.identifier.issn
1345-711X
dc.identifier.uri
http://hdl.handle.net/11336/19712
dc.description.abstract
Sterol carrier protein 2 (SCP2), a small intracellular domain present in all forms of life, binds with high affinity a broad spectrum of lipids. Due to its involvement in the metabolism of long-chain fatty acids and cholesterol uptake, it has been the focus of intense research in mammals and insects; much less characterized are SCP2 from other eukaryotic cells and microorganisms. We report here the X-ray structure of Yarrowia lipolytica SCP2 (YLSCP2) at 2.2 Å resolution in complex with palmitic acid. This is the first fungal SCP2 structure solved, and it consists of the canonical five-stranded β-sheet covered on the internal face by a layer of five α-helices. The overall fold is conserved among the SCP2 family, however, YLSCP2 is most similar to the SCP2 domain of human MFE-2, a bifunctional enzyme acting on peroxisomal β-oxidation. We have identified the common structural elements defining the shape and volume of the large binding cavity in all species characterized. Moreover, we found that the cavity of the SCP2 domains is distinctly formed by carbon atoms, containing neither organized water nor rigid polar interactions with the ligand. These features are in contrast with those of fatty acid binding proteins, whose internal cavities are more polar and contain bound water. The results will help to design experiments to unveil the SCP2 function in very different cellular contexts and metabolic conditions.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Sterol Carrier Protein
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Non-Specific Lipid Binding Protein
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Crystallography
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Yarrowia Lipolytica
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Cholesterol
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B-Oxidation
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Peroxisomes
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Fatty Acids
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
The crystal structure of sterol carrier protein 2 from Yarrowia lipolytica and the evolutionary conservation of a large, non-specific lipid-binding cavity
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-09-05T13:18:12Z
dc.identifier.eissn
1570-0267
dc.journal.volume
14
dc.journal.number
4
dc.journal.pagination
145-153
dc.journal.pais
Alemania
dc.journal.ciudad
Berlín
dc.description.fil
Fil: Pérez de Berti, Federico Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina. Universidad Nacional de Quilmes; Argentina
dc.description.fil
Fil: Capaldi, Stefano. Universita Di Verona; Italia
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Fil: Ferreyra, Raul Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina. Universidad Nacional de Quilmes; Argentina
dc.description.fil
Fil: Burgardt, Noelia Ines. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
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Fil: Acierno, Juan Pablo. Universidad Nacional de Quilmes; Argentina
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Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.description.fil
Fil: Monaco, Hugo L.. Universita Di Verona; Italia
dc.description.fil
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina. Universidad Nacional de Quilmes; Argentina
dc.journal.title
Journal of Structural and Functional Genomics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs10969-013-9166-6
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1007/s10969-013-9166-6


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